Autosomal Recessive Type VII Ehlers-Danlos Syndrome

02/01/1987 - "Morphometric study of cauliflower collagen fibrils in dermatosparaxis of the calves."
02/01/1980 - "Dermatosparaxis in a Himalayan cat: I. Biochemical studies of dermal collagen."
02/01/1980 - "Dermatosparaxis in a Himalayan cat: II. Ultrastructural studies of dermal collagen."
11/19/2022 - "Cross sections of collagen fibrils in post-mortem dermal tissues from 2 of these dogs showed hieroglyphic-like figures similar to those from cases of severe dermatosparaxis in other species. "
03/01/2008 - "Dermatosparaxis is a heritable collagen dysplasia causing skin extensibility and fragility. "

04/01/2006 - "Although Adamts14 lacked developmental tissue-specific expression, it was co-expressed with Adamts2 in mature dermis, which possibly explains the presence of some processed skin procollagen in dermatosparaxis. "
08/24/2001 - "The findings provide an explanation for the sparing of cartilage in dermatosparaxis and, perhaps, for the relative sparing of some procollagen I-containing tissues."
12/01/1984 - "Dermatosparaxis is an inherited disease which results from a deficiency in procollagen aminopropeptidase activity. "
05/01/1973 - "Cell-free synthesis of procollagen: L-929 fibroblasts as a cellular model for dermatosparaxis."
04/01/2006 - "Mutations in ADAMTS2, a procollagen amino-propeptidase, cause severe skin fragility, designated as dermatosparaxis in animals, and a subtype of the Ehlers-Danlos syndrome (dermatosparactic type or VIIC) in humans. "

03/18/1997 - "Deficiencies of the enzyme cause dermatosparaxis in cattle and sheep, and they cause type VIIC Ehlers-Danlos syndrome in humans, heritable disorders characterized by accumulation of pNcollagen and severe skin fragility. "
04/24/1998 - "Dermatosparaxis is a recessive disorder of animals (including man) which is caused by mutations in the gene for the enzyme procollagen N-proteinase and is characterised by extreme skin fragility. "
12/01/1971 - "The enzyme activity is absent in dermatosparaxic connective tissues, thus suggesting that dermatosparaxis is caused by the absence of a normal enzyme function rather than by the production of an abnormal collagen."
01/01/2016 - "The Ehlers-Danlos syndrome (EDS), dermatosparaxis type, is a recessively inherited connective tissue disorder caused by deficient activity of ADAMTS-2, an enzyme that cleaves the aminoterminal propeptide domain of types I, II, and III procollagen. "
01/01/2012 - "Dermatosparaxis (meaning 'tearing of skin'), which has been described in several non-human species, is a disorder of the connective tissue resulting from a deficiency of the enzyme that cleaves the registration peptide off the N-terminal end of collagen after it has been secreted from fibroblasts. "

05/01/1990 - "In one, the cleavage deficiency was due to diminished N-proteinase activity (dermatosparaxis) and in the other case (Ehler's-Danlos syndrome type VIIA) the cleavage site was deleted. "
04/01/2006 - "The data show how evolutionarily related proteases with similar substrate preferences may have distinct biological roles owing to tissue-specific gene expression, and provide insights into collagen biosynthesis and the pathobiology of dermatosparaxis."
01/01/2021 - "Several case of bovine and ovine dermatosparaxis analogous to human Ehlers-Danlos syndrome type VIIC were found to be caused by mutations in the procollagen I N-proteinase (pnPI) or ADAMTS2 gene, though mutations in other sites are likely responsible for other types of dermatosparaxis. "
01/01/2014 - "Several cases of bovine and ovine dermatosparaxis analogous to human Ehlers-Danlos syndrome type VIIC were found to be caused by mutations in the procollagen I N-proteinase (pnPI) or ADAMTS2 gene, though mutations in other sites are likely responsible for other types of dermatosparaxis. "
10/01/2003 - "A 13-year-old patient with dermatosparaxis (Ehlers-Danlos syndrome type VIIC), an autosomal recessive disorder of procollagen-I-N-proteinase, is presented. "

04/01/1993 - "This disease, resulting from a defect in procollagen peptidase, resembles dermatosparaxis in animals. "
01/01/2001 - "ADAMTS2 is a procollagen N-proteinase, and the mutations of its gene are responsible for Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis. "
02/01/1980 - "Dermatosparaxis is a connective tissue disease, primarily of sheep and cattle, that results from deficient activity of the NH2-terminal procollagen peptidase. "
04/24/1998 - "Dermatosparaxis is a recessive disorder of animals (including man) which is caused by mutations in the gene for the enzyme procollagen N-proteinase and is characterised by extreme skin fragility. "
02/01/1977 - "In lathyrism, the toxic agent directly blocks the development of the transverse links in the collagen fibre, while in bovine dermatosparaxis there is a deficiency of procollagen peptidase. "

10/01/1993 - "Dermatosparaxis is an autosomal recessive connective tissue disorder in animals that is caused by abnormal processing of type I procollagen and results in skin laxity and fragility. "
08/01/1992 - "These findings distinguish dermatosparaxis from Ehlers-Danlos syndrome type VII, which results from substrate mutations that prevent proteolytic processing of type I procollagen molecules."
08/01/1992 - "Human dermatosparaxis: a form of Ehlers-Danlos syndrome that results from failure to remove the amino-terminal propeptide of type I procollagen."
08/01/1986 - "The results show that only the conversion of type I procollagen is defective in EDS type VII, and no general defect in procollagen processing can be found in EDS type VII as has been suggested in the case of dermatosparaxis, a connective tissue disorder in animals caused by disturbed procollagen conversion."
02/22/2002 - "Mutations in the ADAMTS2 gene, the aminopropeptidase of procollagen I and II, result in the accumulation of non-fully processed type I procollagen, causing human Ehlers-Danlos syndrome type VIIC and animal dermatosparaxis. "

07/01/2012 - "Mutations in type V and type III collagen cause classic or vascular EDS respectively, while mutations involving the processing of type I collagen are involved in the kyphoscoliosis, arthrochalasis and dermatosparaxis type of EDS. "
01/01/1995 - "Recent advances in the molecular analysis of EDS have identify defects responsible for EDS VI (homozygous and compound heterozygous mutations in the lysyl-hydroxylase gene), EDS VIIA and EDS VIIB (mutations in the type I collagene genes), EDS VIIC (deficiency of procollagen N-proteinase), EDS IX (mutations in the MNK gene), and EDS IV (mutations in the type III collagen gene). "
05/23/2003 - "Thus, the dogma that procollagen I and procollagen III N-proteinase activities are provided by separate enzymes appears to be false, whereas the phenotypes of dermatosparaxis and Ehlers-Danlos VIIC may arise from defects in both type I and type III collagen biosynthesis."
09/01/1993 - "Recent advances in the molecular analysis of EDS have identified defects responsible for EDS IV (mutations in the type III collagen gene), EDS VI (homozygous and compound heterozygous mutations in the lysyl hydroxylase gene), EDS VIIA and VIIB (mutations in the type I collagen genes), EDS VIIC (deficiency of procollagen N-proteinase), and EDS IX (decreased lysyl oxidase activity). "

02/01/2015 - "Mutations in the ADAM metallopeptidase with thrombospondin type 1 motif, 2 (ADAMTS2) locus, are involved in the development of dermatosparaxis in humans, cattle and the dorper sheep breed; consequently, this locus was investigated in the flock. "
08/01/2012 - "We have used polymerase chain reaction-single-strand conformational polymorphism analysis to investigate variation in exon 2 of the ADAM metalloproteinase with thrombospondin type I motif, 2 (ADAMTS2) gene in 598 sheep, including three white Dorper lambs that had a pathology consistent with dermatosparaxis. "
05/23/2003 - "The metalloproteinase ADAMTS-2 has procollagen I N-proteinase activity capable of cleaving procollagens I and II N-propeptides in vitro, whereas mutations in the ADAMTS-2 gene in dermatosparaxis and Ehlers-Danlos syndrome VIIC show this enzyme to be responsible in vivo for most biosynthetic processing of procollagen I N-propeptides in skin. "

07/01/2012 - "Mutations in type V and type III collagen cause classic or vascular EDS respectively, while mutations involving the processing of type I collagen are involved in the kyphoscoliosis, arthrochalasis and dermatosparaxis type of EDS. "
03/01/2008 - "Mutations in genes encoding fibrillar collagens or collagen-modifying enzymes have been identified in most forms of EDS, including the classic and vascular subtypes (collagen type V and III, respectively), and the rare arthrochalasis, kyphoscoliosis and dermatosparaxis variants (type I collagen defects). "
09/01/1993 - "Recent advances in the molecular analysis of EDS have identified defects responsible for EDS IV (mutations in the type III collagen gene), EDS VI (homozygous and compound heterozygous mutations in the lysyl hydroxylase gene), EDS VIIA and VIIB (mutations in the type I collagen genes), EDS VIIC (deficiency of procollagen N-proteinase), and EDS IX (decreased lysyl oxidase activity). "

01/01/1991 - "Dermal fibroblasts from sheep exhibiting a mild form of dermatosparaxis were able to contract reconstituted, fibrillar collagen gels at the same rate as control dermal fibroblasts, indicating a normal interaction between the cells and a collagenous matrix. "
03/01/2008 - "Mutations in genes encoding fibrillar collagens or collagen-modifying enzymes have been identified in most forms of EDS, including the classic and vascular subtypes (collagen type V and III, respectively), and the rare arthrochalasis, kyphoscoliosis and dermatosparaxis variants (type I collagen defects). "